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http://purl.uniprot.org/citations/15733859http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15733859http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15733859http://www.w3.org/2000/01/rdf-schema#comment"Bcl-2 contains an unusually long loop between the first and the second helices. This loop has been shown to be highly flexible based on NMR and X-ray crystallographic analyses of this region. Bcl-2 is regulated at the posttranslational level through phosphorylation of specific residues within the flexible loop. The biological role and posttranslational modifications of the loop of Bcl-2 is currently unclear. FK-506 binding protein 38 (FKBP38) has been reported to interact with Bcl-2, suggesting that FKBP38 could act as a docking molecule to localize Bcl-2 at the mitochondrial membrane [Shirane, M. and Nakayama, K.I. (2003) Inherent calcineurin inhibitor FKBP38 targets Bcl-2 to mitochondria and inhibits apoptosis. Nat. Cell Biol. 5, 28-37]. Here, we investigated the molecular interaction between FKBP38 and Bcl-2, and demonstrated that Bcl-2 interacts with FKBP38 through the unstructured loop, and the interaction appears to regulate phosphorylation in the loop of Bcl-2."xsd:string
http://purl.uniprot.org/citations/15733859http://purl.org/dc/terms/identifier"doi:10.1016/j.febslet.2005.01.053"xsd:string
http://purl.uniprot.org/citations/15733859http://purl.org/dc/terms/identifier"doi:10.1016/j.febslet.2005.01.053"xsd:string
http://purl.uniprot.org/citations/15733859http://purl.uniprot.org/core/author"Chia J."xsd:string
http://purl.uniprot.org/citations/15733859http://purl.uniprot.org/core/author"Chia J."xsd:string
http://purl.uniprot.org/citations/15733859http://purl.uniprot.org/core/author"Kang C.B."xsd:string
http://purl.uniprot.org/citations/15733859http://purl.uniprot.org/core/author"Kang C.B."xsd:string
http://purl.uniprot.org/citations/15733859http://purl.uniprot.org/core/author"Yoon H.S."xsd:string
http://purl.uniprot.org/citations/15733859http://purl.uniprot.org/core/author"Yoon H.S."xsd:string
http://purl.uniprot.org/citations/15733859http://purl.uniprot.org/core/author"Tai J."xsd:string
http://purl.uniprot.org/citations/15733859http://purl.uniprot.org/core/author"Tai J."xsd:string
http://purl.uniprot.org/citations/15733859http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15733859http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15733859http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/15733859http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/15733859http://purl.uniprot.org/core/pages"1469-1476"xsd:string
http://purl.uniprot.org/citations/15733859http://purl.uniprot.org/core/pages"1469-1476"xsd:string
http://purl.uniprot.org/citations/15733859http://purl.uniprot.org/core/title"The flexible loop of Bcl-2 is required for molecular interaction with immunosuppressant FK-506 binding protein 38 (FKBP38)."xsd:string
http://purl.uniprot.org/citations/15733859http://purl.uniprot.org/core/title"The flexible loop of Bcl-2 is required for molecular interaction with immunosuppressant FK-506 binding protein 38 (FKBP38)."xsd:string
http://purl.uniprot.org/citations/15733859http://purl.uniprot.org/core/volume"579"xsd:string
http://purl.uniprot.org/citations/15733859http://purl.uniprot.org/core/volume"579"xsd:string
http://purl.uniprot.org/citations/15733859http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15733859
http://purl.uniprot.org/citations/15733859http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15733859